How does the hydrophobic effect influence protein folding? In an aqueous environment, nonpolar portions of the...
How does the hydrophobic effect influence protein folding?
In an aqueous environment, nonpolar portions of the molecule
A) are generally exposed to solvent and interact effectively with water.
B) interact with polar portions in the interior of the protein.
C) can be placed on the surface of the molecule only if hydrogen bonded to water.
D) are found in the interior of the protein, away from water, which preserves the entropy of water in solution.
Homework Answers
Answer-
In an aqueous environment, nonpolar portions of the molecule D) are found in the interior of the protein, away from water, which preserves the entropy of water in solution.
Water is polar molecule. Oxygen is slightly electronegative than hydrogen. So, oxygen nucleus attracts electrons more strongly than hydrogen nucleus. Therefore the sharing of electrons between H and O is unequal. This unequal sharing of electrons creates 2 electric dipoless in water molecule. O atom bears a partial negative charge and hydrogen bears a partial positive charge. This results in formation of hydrogen bond between O atom of one water molecule and hydrogen atom of another nearby water molecule. Hydrophobes are nonpolar, they have long carbon chains which do not interact with water. When they are placed in aqueous solution, they tend to clump together rather than distributing themslves in water solution.
Hydrophobic effects in Protein folding
When proteins are placed in water solution they fold into three-dimentional structures. Much of this driving forces come from hydrophobic effect. Protein contains several hydrophobic amino acids (alanine, glycine, methionine, leucine, valine etc.). In aqueous solution these hydrophobic amino acids are buried inside the core portion. Water tends to form a cage around protein which leads to a decrease in entropy.
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How does the hydrophobic effect influence protein folding?
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Protein folding and lipid-bilayer formation result in decreased entropy for a protein molecule and bilayer components. The decrease entropy of the surrounding entropy is balanced by a large increase in the OTemperature Salt solutions Pressure Water molecules Water's ability to dissolve a wide variety of molecules is important, but more important is the hydrophobic effect, which drives the aggregation of nonpolar molecules and plays a role in the folding of proteins and formation of lipid bilayers. What forces drive the...
1. Which of the following statements is consistent with the
structural motifs in 1OPF?
This protein has tertiary structure, where each subunit is a
large parallel beta barrel.
This protein has quaternary structure, where each subunit is a
large antiparallel beta barrel.
This protein has tertiary structure, where each subunit is a
large antiparallel beta barrel.
This protein has quaternary structure, where each subunit is a
large parallel beta barrel.
3. Given the information in the PDB entry for 1OPF,...
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